ID A0A3S1C7R6_ANAVA Unreviewed; 835 AA.
AC A0A3S1C7R6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RUS96825.1};
GN ORFNames=DSM107003_22310 {ECO:0000313|EMBL:RUS96825.1};
OS Trichormus variabilis SAG 1403-4b.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
OC Nostocaceae; Trichormus.
OX NCBI_TaxID=447716 {ECO:0000313|EMBL:RUS96825.1, ECO:0000313|Proteomes:UP000276103};
RN [1] {ECO:0000313|EMBL:RUS96825.1, ECO:0000313|Proteomes:UP000276103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 1403-4b {ECO:0000313|EMBL:RUS96825.1,
RC ECO:0000313|Proteomes:UP000276103};
RX PubMed=30590650;
RA Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA Neumann-Schaal M., Petersen J.;
RT "Day and night: Metabolic profiles and evolutionary relationships of six
RT axenic non-marine cyanobacteria.";
RL Genome Biol. Evol. 0:0-0(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans,octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUS96825.1}.
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DR EMBL; RSCM01000006; RUS96825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S1C7R6; -.
DR Proteomes; UP000276103; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:TreeGrafter.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR050396; Glycosyltr_51/Transpeptidase.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000276103};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..252
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 378..650
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 725..797
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 297..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 92848 MW; E58D641C7AFF99FC CRC64;
MNFKPRNLKT PTLCVSATLR EIKSYFRYIH RYKPIKIILA VIIFCLIVRL MPYLAPIHSV
DISQKQLAME FTDRNGLPLG TILTHDQEHT AIIPLTQISP QFINAILAAE DSSFYQHGAL
DLKAIFRAIK EAIHAKKIVS GASTITMQLA RMLDNSPRNI SGKLQEIWLS WRLTAGMNKN
EILSAYINRL PMGGNIYGVE AAARIYFSIS ASDLNLAQAS LLAAIPNNPT YFNPYEHWER
LKKRQKYVLN RLVQEGYISH LEAERIYTEK VVFQSRQKGI IAAPHFLFWL ATQSTPPLTP
PRKRGGGLEL SSRKRGGGLE LSSSKRGGGL ELSSLKGGGG LESSPIQTTI NRPLQQFVEA
QVQQVISTLA EKNVHDAAAV VIDNYSGEVL AYVGSPDYFN EVKLGRNDGV QALRQPGSTL
KPFVYELALE KGAIKPNSIL ADVPSHYAIP GAKLYSPTDY TNSFLGPVRV RVALANSLNV
PAVKVLEKVG VQTFLNRLHE LGFAHLNQSV EYYGLGLTLG SGEVSLWELA RAYVTMARLG
ETTPLLTILT ELTEPQTPTP HSPSKKPTWQ LIIDILSDRY ARATAFGVDS VLNLPFPTAV
KTGTSSNYRD TWTVGFSTDY TVATWVGNFN GEPMRQVSGV TGAAPLWNRI MLHLHEHQSP
AYFPHPEAMV QLPICATSGL KPTPDCHSVV QEYFSPEDKI AYEHQQNFHL PPEYDEWLAK
QPQFNSFAAN QLRILSPRDG DLFLVNPGAE GQQKLEFKLA GAFNQPIEWW LNGKKLSTQS
ANALFWHLRP GSWTLEARSN QMSDRISFQV ELANKQPIRS GFSVVNSTKS PDSGH
//
